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Fes/c-Fes Tyrosine Protein Kinase Targeted Library

The non-receptor tyrosine kinase feline sarcoma oncogene (FES) and FES-related kinase (FER), due to their unique structural organization, comprise a special subfamily of protein-tyrosine kinases (PTKs). They signal downstream of several classes of receptors involved in regulating hematopoietic cell development, survival, migration, and inflammatory mediator release [1-2]. To clarify the roles of c-Fes as the dominant oncogene vs tumor suppressors depending upon the cellular context selective small molecule inhibitors are vitally important.

In this context the Life Chemicals cheminformatics team presents a new proprietary Fes/c-Fes Tyrosine Protein Kinase Targeted Library of over 1,100 drug-like screening compounds selected by molecular docking. The compound selection details are described below.

Additionally, we offer a related SH2 Domain Focused Library of 2,200 drug-like screening compounds with predicted affinity to these Src homology 2 domains, designed by a receptor-based approach: pharmacophore modeling using X-ray data of SH2-inhibitor complexes.

The compound selection can be customized based on your requirements, cherry picking is available.

Please, contact us at for any additional information and price quotations.

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Background information

Recently, FES/FER have been implicated in growth and survival signaling in leukemias driven by oncogenic KIT and FLT3 receptors. With a further definition of their roles in immune cells and their progenitors, FES/FER may emerge as relevant therapeutic targets in inflammatory diseases and leukemias [1].

The structural organization of c-Fes is distinct from other non-receptor tyrosine kinases, such as c-Src and c-Abl [4]. The unique N-terminal region features a Fes/CIP4 homology (FCH) domain, followed by two-coiled coil motifs, a central Src-homology 2 (SH2) domain, and a C-terminal kinase catalytic domain [3]. FES SH2 domain binds phosphorylated tyrosine residues and functions as a protein interaction domain, which may lead to further phosphorylation of the same ligand or other ligand-associated proteins.

Compound selection

The Fes/c-Fes Tyrosine Protein Kinase Targeted Library of 1,100 drug-like screening compounds that are potential modulators of tyrosine-protein kinases FES was selected from the proprietary HTS Compound Collection by means of molecular docking.

Key features:

  • Method: high-throughput virtual screening (docking), molecular fitting
  • X-Ray data used: 4E93
  • Constraints: no
  • Filters used: PAINS, toxic, reactive
  • Number of compounds selected: 1158

Spatial structure binding site of the complex of FES with lead docking molecule F6474-8027 (docking score = -8.738)

Figure 1. Spatial structure binding site of the complex of FES with lead docking molecule F6474-8027 (docking score = -8.738)


  1. Craig AW. FES/FER kinase signaling in hematopoietic cells and leukemias. Front Biosci (Landmark Ed). 2012 Jan 1;17(3):861-75. doi: 10.2741/3961. PMID: 22201778.
  2. van der Wel, T., Hilhorst, R., den Dulk, H. et al. Chemical genetics strategy to profile kinase target engagement reveals role of FES in neutrophil phagocytosis. Nat Commun 11, 3216 (2020).
  3. Hellwig S, Miduturu CV, Kanda S, Zhang J, Filippakopoulos P, Salah E, Deng X, Choi HG, Zhou W, Hur W, Knapp S, Gray NS, Smithgall TE. Small-molecule inhibitors of the c-Fes protein-tyrosine kinase. Chem Biol. 2012 Apr 20;19(4):529-40. doi: 10.1016/j.chembiol.2012.01.020. PMID: 22520759; PMCID: PMC3334838.
  4. Hellwig S, Smithgall TE. Structure and regulation of the c-Fes protein-tyrosine kinase. Front Biosci. 2011;17:3146–3155.
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